ID A3JWA1_9RHOB Unreviewed; 806 AA.
AC A3JWA1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EBA02115.1};
GN ORFNames=RB2150_00380 {ECO:0000313|EMBL:EBA02115.1};
OS Rhodobacteraceae bacterium HTCC2150.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA02115.1, ECO:0000313|Proteomes:UP000004731};
RN [1] {ECO:0000313|EMBL:EBA02115.1, ECO:0000313|Proteomes:UP000004731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA02115.1,
RC ECO:0000313|Proteomes:UP000004731};
RX PubMed=20889754; DOI=10.1128/JB.01088-10;
RA Kang I., Oh H.M., Vergin K.L., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of the marine alphaproteobacterium HTCC2150, assigned to
RT the Roseobacter clade.";
RL J. Bacteriol. 192:6315-6316(2010).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EBA02115.1}.
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DR EMBL; AAXZ01000013; EBA02115.1; -; Genomic_DNA.
DR AlphaFoldDB; A3JWA1; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0665; Bacteria.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000004731; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR13847:SF187; DIMETHYLGLYCINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000004731}.
FT DOMAIN 7..364
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 367..420
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 424..692
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 732..798
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 806 AA; 89301 MW; 7E5B5106CF14ADA3 CRC64;
MRTQAQAVVI GGGVIGCSIL YHLTKLGWSD VVLLERDELT SGSTWHAAAN IHGLHDSTNI
SRIQHYTMNL YNDLEAETGQ SCGVFQPGSL YLAQTEEREH QLRLQAAKAK LYGMNFYEIS
IEEAQKLHPM VNYDGIRCVM YEPDGGNVDP SGVTSAYAAG ARQNGAEINR FTPVTATEQQ
TDGSWIVKTP KGDIHTQWVV NAAGLWGREV AALAGITLPL QPTEHQYFVT ETIQEIADAP
NRLPSVSDRD GEYYLRQEGQ GLLVGAYEKN MKFWAEDGTP LDFAHELFAD DLERIEDNMM
NAIERVPAVG EAGIKRVING PMIWSPDANV LFGPLPELEN YFCCNGIIPG FSQSGGMGLM
AAQWIIEGET QYDMYAWDVA RFGDWADKEF TKAKVEDQYS HRFAIHFPNE ERSAGRPCRV
RPIYEMQKQM GAVFGLNVGW EHPLWFSDKP DTQDTNGFTR QNWWGPVGQE CKMLRQNAGI
IDISNFAKYI CKGPGAADWL NALFANNMPK AVGRSCLTPL IGKRGGIAGD FTVTRVAEDE
FWIIGSGLAE RYHTRFFKQI PLPHGTTFES HTEAFCGFNV AGPKSRDILQ RLTNTSLATA
DFPFMRSKMV DLAGIELLAL RVSFTGDLGW ELHCKAEDQM RLYETLLEAG KEFGSGPVGS
RALMSLRVEK GYGSWSREYS PEYWPQEVGL DRLCKMDKNF LNKSAAAETM SNAPREDLVL
LHLEEADVNA SNADATGGEP IFMNGKGIGR VTSGTYGYTV GMSLALGYVK GAKPGDRVQV
MVLGTPHNAV ILTEPPFDPK GERLRA
//